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P37617

- ATZN_ECOLI

UniProt

P37617 - ATZN_ECOLI

Protein

Lead, cadmium, zinc and mercury-transporting ATPase

Gene

zntA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Involved in export of lead, cadmium, zinc and mercury.

    Catalytic activityi

    ATP + H2O + Cd2+(In) = ADP + phosphate + Cd2+(Out).
    ATP + H2O + Zn2+(In) = ADP + phosphate + Zn2+(Out).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi58 – 581Zinc
    Metal bindingi59 – 591Zinc
    Metal bindingi62 – 621Zinc
    Active sitei436 – 43614-aspartylphosphate intermediateBy similarity
    Metal bindingi628 – 6281MagnesiumPROSITE-ProRule annotation
    Metal bindingi632 – 6321MagnesiumPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATPase activity Source: EcoliWiki
    2. ATP binding Source: UniProtKB-KW
    3. cadmium-exporting ATPase activity Source: EcoCyc
    4. cobalt ion transmembrane transporter activity Source: EcoCyc
    5. lead ion transmembrane transporter activity Source: EcoCyc
    6. metal ion binding Source: UniProtKB-KW
    7. nickel cation transmembrane transporter activity Source: EcoCyc
    8. zinc-exporting ATPase activity Source: EcoCyc

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cadmium ion transmembrane transport Source: GOC
    3. cobalt ion transport Source: EcoCyc
    4. detoxification of zinc ion Source: EcoliWiki
    5. lead ion transport Source: EcoCyc
    6. nickel cation transmembrane transport Source: GOC
    7. response to cadmium ion Source: EcoliWiki
    8. zinc ion transmembrane transport Source: GOC
    9. zinc ion transport Source: EcoliWiki

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Cadmium, Magnesium, Mercury, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:YHHO-MONOMER.
    ECOL316407:JW3434-MONOMER.
    MetaCyc:YHHO-MONOMER.
    SABIO-RKP37617.

    Protein family/group databases

    TCDBi3.A.3.6.2. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lead, cadmium, zinc and mercury-transporting ATPase (EC:3.6.3.3, EC:3.6.3.5)
    Gene namesi
    Name:zntA
    Synonyms:yhhO
    Ordered Locus Names:b3469, JW3434
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12215. zntA.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: EcoCyc
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 732732Lead, cadmium, zinc and mercury-transporting ATPasePRO_0000046332Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP37617.
    PRIDEiP37617.

    Expressioni

    Gene expression databases

    GenevestigatoriP37617.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-12947N.
    IntActiP37617. 8 interactions.
    MINTiMINT-1256950.
    STRINGi511145.b3469.

    Structurei

    Secondary structure

    1
    732
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi48 – 569
    Helixi62 – 7110
    Beta strandi73 – 8210
    Turni83 – 864
    Beta strandi87 – 948
    Helixi97 – 10711
    Beta strandi110 – 1134

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MWYNMR-A46-118[»]
    1MWZNMR-A46-118[»]
    ProteinModelPortaliP37617.
    SMRiP37617. Positions 46-732.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37617.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 124124PeriplasmicSequence AnalysisAdd
    BLAST
    Topological domaini146 – 19146CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini213 – 356144PeriplasmicSequence AnalysisAdd
    BLAST
    Topological domaini378 – 3836CytoplasmicSequence Analysis
    Topological domaini405 – 46157PeriplasmicSequence AnalysisAdd
    BLAST
    Topological domaini483 – 632150CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini654 – 69340PeriplasmicSequence AnalysisAdd
    BLAST
    Topological domaini715 – 73218CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei125 – 14521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei192 – 21221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei357 – 37721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei384 – 40421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei462 – 48221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei633 – 65321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei694 – 71421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini49 – 11365HMAPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 HMA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2217.
    HOGENOMiHOG000250399.
    KOiK01534.
    OMAiSGMDCPS.
    OrthoDBiEOG6742RM.
    PhylomeDBiP37617.

    Family and domain databases

    Gene3Di2.70.150.10. 1 hit.
    3.40.1110.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiIPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR027256. Cation_transp_P-typ_ATPase_IB.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    IPR017969. Heavy-metal-associated_CS.
    IPR006121. HeavyMe-assoc_HMA.
    [Graphical view]
    PfamiPF00122. E1-E2_ATPase. 1 hit.
    PF00403. HMA. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    PR00120. HATPASE.
    SUPFAMiSSF55008. SSF55008. 1 hit.
    SSF56784. SSF56784. 2 hits.
    TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 1 hit.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    PS01047. HMA_1. 1 hit.
    PS50846. HMA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P37617-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTPDNHGKK APQFAAFKPL TTVQNANDCC CDGACSSTPT LSENVSGTRY    50
    SWKVSGMDCA ACARKVENAV RQLAGVNQVQ VLFATEKLVV DADNDIRAQV 100
    ESALQKAGYS LRDEQAAEEP QASRLKENLP LITLIVMMAI SWGLEQFNHP 150
    FGQLAFIATT LVGLYPIARQ ALRLIKSGSY FAIETLMSVA AIGALFIGAT 200
    AEAAMVLLLF LIGERLEGWA ASRARQGVSA LMALKPETAT RLRKGEREEV 250
    AINSLRPGDV IEVAAGGRLP ADGKLLSPFA SFDESALTGE SIPVERATGD 300
    KVPAGATSVD RLVTLEVLSE PGASAIDRIL KLIEEAEERR APIERFIDRF 350
    SRIYTPAIMA VALLVTLVPP LLFAASWQEW IYKGLTLLLI GCPCALVIST 400
    PAAITSGLAA AARRGALIKG GAALEQLGRV TQVAFDKTGT LTVGKPRVTA 450
    IHPATGISES ELLTLAAAVE QGATHPLAQA IVREAQVAEL AIPTAESQRA 500
    LVGSGIEAQV NGERVLICAA GKHPADAFTG LINELESAGQ TVVLVVRNDD 550
    VLGVIALQDT LRADAATAIS ELNALGVKGV ILTGDNPRAA AAIAGELGLE 600
    FKAGLLPEDK VKAVTELNQH APLAMVGDGI NDAPAMKAAA IGIAMGSGTD 650
    VALETADAAL THNHLRGLVQ MIELARATHA NIRQNITIAL GLKGIFLVTT 700
    LLGMTGLWLA VLADTGATVL VTANALRLLR RR 732
    Length:732
    Mass (Da):76,840
    Last modified:October 1, 1994 - v1
    Checksum:i25476EA830786465
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00039 Genomic DNA. Translation: AAB18444.1.
    U00096 Genomic DNA. Translation: AAC76494.1.
    AP009048 Genomic DNA. Translation: BAE77824.1.
    PIRiS47688.
    RefSeqiNP_417926.1. NC_000913.3.
    YP_491965.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76494; AAC76494; b3469.
    BAE77824; BAE77824; BAE77824.
    GeneIDi12933927.
    947972.
    KEGGiecj:Y75_p3709.
    eco:b3469.
    PATRICi32122382. VBIEscCol129921_3568.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00039 Genomic DNA. Translation: AAB18444.1 .
    U00096 Genomic DNA. Translation: AAC76494.1 .
    AP009048 Genomic DNA. Translation: BAE77824.1 .
    PIRi S47688.
    RefSeqi NP_417926.1. NC_000913.3.
    YP_491965.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MWY NMR - A 46-118 [» ]
    1MWZ NMR - A 46-118 [» ]
    ProteinModelPortali P37617.
    SMRi P37617. Positions 46-732.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-12947N.
    IntActi P37617. 8 interactions.
    MINTi MINT-1256950.
    STRINGi 511145.b3469.

    Protein family/group databases

    TCDBi 3.A.3.6.2. the p-type atpase (p-atpase) superfamily.

    Proteomic databases

    PaxDbi P37617.
    PRIDEi P37617.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76494 ; AAC76494 ; b3469 .
    BAE77824 ; BAE77824 ; BAE77824 .
    GeneIDi 12933927.
    947972.
    KEGGi ecj:Y75_p3709.
    eco:b3469.
    PATRICi 32122382. VBIEscCol129921_3568.

    Organism-specific databases

    EchoBASEi EB2129.
    EcoGenei EG12215. zntA.

    Phylogenomic databases

    eggNOGi COG2217.
    HOGENOMi HOG000250399.
    KOi K01534.
    OMAi SGMDCPS.
    OrthoDBi EOG6742RM.
    PhylomeDBi P37617.

    Enzyme and pathway databases

    BioCyci EcoCyc:YHHO-MONOMER.
    ECOL316407:JW3434-MONOMER.
    MetaCyc:YHHO-MONOMER.
    SABIO-RK P37617.

    Miscellaneous databases

    EvolutionaryTracei P37617.
    PROi P37617.

    Gene expression databases

    Genevestigatori P37617.

    Family and domain databases

    Gene3Di 2.70.150.10. 1 hit.
    3.40.1110.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProi IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR027256. Cation_transp_P-typ_ATPase_IB.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    IPR017969. Heavy-metal-associated_CS.
    IPR006121. HeavyMe-assoc_HMA.
    [Graphical view ]
    Pfami PF00122. E1-E2_ATPase. 1 hit.
    PF00403. HMA. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    PR00120. HATPASE.
    SUPFAMi SSF55008. SSF55008. 1 hit.
    SSF56784. SSF56784. 2 hits.
    TIGRFAMsi TIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 1 hit.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    PS01047. HMA_1. 1 hit.
    PS50846. HMA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
      Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
      Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase."
      Rensing C., Mitra B., Rosen B.P.
      Proc. Natl. Acad. Sci. U.S.A. 94:14326-14331(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. "Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase."
      Beard S.J., Hashim R., Membrillo-Hernandez J., Hughes M.N., Poole R.K.
      Mol. Microbiol. 25:883-891(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli."
      Sharma R., Rensing C., Rosen B.P., Mitra B.
      J. Biol. Chem. 275:3873-3878(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "Global topology analysis of the Escherichia coli inner membrane proteome."
      Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
      Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
      Strain: K12 / MG1655 / ATCC 47076.
    8. "A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118)."
      Banci L., Bertini I., Ciofi-Baffoni S., Finney L.A., Outten C.E., O'Halloran T.V.
      J. Mol. Biol. 323:883-897(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 46-118 IN APO AND ZINC-BOUND FORMS.

    Entry informationi

    Entry nameiATZN_ECOLI
    AccessioniPrimary (citable) accession number: P37617
    Secondary accession number(s): Q2M7D2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3